Evidence map›Paper›PMID 9412463›Full record

ArticleThe Journal of cell biology1997

Analysis of the interactions of preproteins with the import machinery over the course of protein import into chloroplasts.

A Kouranov, D J Schnell

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
4.4field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

73 citing papers in PubMed, 214 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Genetic Mapping of theFrontiers in plant science · 2022
    Article
  5. Coexpressed subunits of dual genetic origin define a conserved supercomplex mediating essential protein import into chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Article
  7. Review
  8. Review
  9. A Protochlorophyllide (Pchlide)Frontiers in plant science · 2019
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Three proteins mediate import of transit sequence-less precursors into the inner envelope of chloroplasts in Arabidopsis thaliana.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  20. An essential role for chloroplast heat shock protein 90 (Hsp90C) in protein import into chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article

13 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

A KouranovDepartment of Biological Sciences, Rutgers University, Newark, New Jersey 07102, USA.
D J Schnell
Rutgers, The State University of New Jersey · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have investigated the interactions of two nuclear-encoded preproteins with the chloroplast protein import machinery at three stages in import using a label-transfer crosslinking approach. During energy-independent binding at the outer envelope membrane, preproteins interact with three known components of the outer membrane translocon complex, Toc34, Toc75, and Toc86. Although Toc75 and Toc86 are known to associate with preproteins during import, a role for Toc34 in preprotein binding previously had not been observed. The interaction of Toc34 with preproteins is regulated by the binding, but not hydrolysis of GTP. These data provide the first evidence for a direct role for Toc34 in import, and provide insights into the function of GTP as a regulator of preprotein recognition. Toc75 and Toc86 are the major targets of cross-linking upon insertion of preproteins across the outer envelope membrane, supporting the proposal that both proteins function in translocation at the outer membrane as well as preprotein recognition. The inner membrane proteins, Tic(21) and Tic22, and a previously unidentified protein of 14 kD are the major targets of crosslinking during the late stages in import. These data provide additional support for the roles of these components during protein translocation across the inner membrane. Our results suggest a defined sequence of molecular interactions that result in the transport of nuclear-encoded preproteins from the cytoplasm into the stroma of chloroplasts.

Indexed as

Biological TransportChloroplastsCross-Linking ReagentsFerredoxinsGuanosine TriphosphateHistone-Lysine N-MethyltransferaseIntracellular MembranesMembrane ProteinsNuclear ProteinsPisum sativumProtein PrecursorsRecombinant Fusion ProteinsStaphylococcal Protein ACross-Linking ReagentsFerredoxinsGuanosine TriphosphateHistone-Lysine N-MethyltransferaseMembrane ProteinsNuclear ProteinspreferredoxinProtein PrecursorsRecombinant Fusion Proteinsribulose-1,5-bisphosphate carboxylase-oxygenase large subunit epsilonN-methyltransferaseStaphylococcal Protein A

Identifiers

PMID9412463
PMCPMC2132644
OpenAlexW2135166311

What OpenQuestion holds

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LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.